LYAR_HUMAN - dbPTM
LYAR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYAR_HUMAN
UniProt AC Q9NX58
Protein Name Cell growth-regulating nucleolar protein
Gene Name LYAR
Organism Homo sapiens (Human).
Sequence Length 379
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm . Cell projection, cilium, photoreceptor outer segment . Component of pre-ribosomal particles, including pre-40S, pre-60S and pre-90S (PubMed:24495227). Associated with cytoplasmic ribosomes, but not polysomes
Protein Description Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs. [PubMed: 24495227 Also acts at the level of transcription regulation. Along with PRMT5, binds the gamma-globin (HBG1/HBG2) promoter and represses its expression]
Protein Sequence MVFFTCNACGESVKKIQVEKHVSVCRNCECLSCIDCGKDFWGDDYKNHVKCISEDQKYGGKGYEGKTHKGDIKQQAWIQKISELIKRPNVSPKVRELLEQISAFDNVPRKKAKFQNWMKNSLKVHNESILDQVWNIFSEASNSEPVNKEQDQRPLHPVANPHAEISTKVPASKVKDAVEQQGEVKKNKRERKEERQKKRKREKKELKLENHQENSRNQKPKKRKKGQEADLEAGGEEVPEANGSAGKRSKKKKQRKDSASEEEAHVGAGKRKRRHSEVETDSKKKKMKLPEHPEGGEPEDDEAPAKGKFNWKGTIKAILKQAPDNEITIKKLRKKVLAQYYTVTDEHHRSEEELLVIFNKKISKNPTFKLLKDKVKLVK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationTCNACGESVKKIQVE
EECCCCCCCCEEEEE		25.2325159151
14SumoylationNACGESVKKIQVEKH
CCCCCCCCEEEEEEC		54.1328112733
14MalonylationNACGESVKKIQVEKH
CCCCCCCCEEEEEEC		54.1326320211
14AcetylationNACGESVKKIQVEKH
CCCCCCCCEEEEEEC		54.1330584187
202-HydroxyisobutyrylationVKKIQVEKHVSVCRN
CCEEEEEECHHHCCC		50.91-
20AcetylationVKKIQVEKHVSVCRN
CCEEEEEECHHHCCC		50.9121466224
38AcetylationLSCIDCGKDFWGDDY
EEEECCCCCCCCCCC		56.9626051181
46AcetylationDFWGDDYKNHVKCIS
CCCCCCCCCCEEECC		47.7926051181
50UbiquitinationDDYKNHVKCISEDQK
CCCCCCEEECCCCCC		20.4929967540
502-HydroxyisobutyrylationDDYKNHVKCISEDQK
CCCCCCEEECCCCCC		20.49-
50AcetylationDDYKNHVKCISEDQK
CCCCCCEEECCCCCC		20.4925953088
57AcetylationKCISEDQKYGGKGYE
EECCCCCCCCCCCCC		59.1826051181
61AcetylationEDQKYGGKGYEGKTH
CCCCCCCCCCCCCCC		54.6923749302
73UbiquitinationKTHKGDIKQQAWIQK
CCCCCCHHHHHHHHH		40.8929967540
80UbiquitinationKQQAWIQKISELIKR
HHHHHHHHHHHHHHC		38.782097226
91PhosphorylationLIKRPNVSPKVRELL
HHHCCCCCHHHHHHH		26.1630576142
932-HydroxyisobutyrylationKRPNVSPKVRELLEQ
HCCCCCHHHHHHHHH		46.55-
93UbiquitinationKRPNVSPKVRELLEQ
HCCCCCHHHHHHHHH		46.5529967540
113AcetylationNVPRKKAKFQNWMKN
CCCHHHHHHHHHHHH		57.2625953088
121PhosphorylationFQNWMKNSLKVHNES
HHHHHHHHHHHCCHH		24.8525599653
128PhosphorylationSLKVHNESILDQVWN
HHHHCCHHHHHHHHH		33.4922199227
138PhosphorylationDQVWNIFSEASNSEP
HHHHHHHHHHCCCCC		28.5820068231
141PhosphorylationWNIFSEASNSEPVNK
HHHHHHHCCCCCCCH		36.5220068231
143PhosphorylationIFSEASNSEPVNKEQ
HHHHHCCCCCCCHHH		40.5620068231
166PhosphorylationANPHAEISTKVPASK
CCCCCCCCCCCCHHH		17.4328555341
167PhosphorylationNPHAEISTKVPASKV
CCCCCCCCCCCHHHH		41.5428555341
168AcetylationPHAEISTKVPASKVK
CCCCCCCCCCHHHHH		39.1625953088
172PhosphorylationISTKVPASKVKDAVE
CCCCCCHHHHHHHHH		31.7323403867
173AcetylationSTKVPASKVKDAVEQ
CCCCCHHHHHHHHHH		56.2425953088
1732-HydroxyisobutyrylationSTKVPASKVKDAVEQ
CCCCCHHHHHHHHHH		56.24-
185AcetylationVEQQGEVKKNKRERK
HHHHCHHHHHHHHHH		46.4526051181
204UbiquitinationKKRKREKKELKLENH
HHHHHHHHHHHHHHH		64.6224816145
207SumoylationKREKKELKLENHQEN
HHHHHHHHHHHHHHH		55.64-
207SumoylationKREKKELKLENHQEN
HHHHHHHHHHHHHHH		55.6428112733
215PhosphorylationLENHQENSRNQKPKK
HHHHHHHCCCCCCCC		31.6820068231
222UbiquitinationSRNQKPKKRKKGQEA
CCCCCCCCCCCCCCC		77.3524816145
225UbiquitinationQKPKKRKKGQEADLE
CCCCCCCCCCCCCHH		70.6124816145
244PhosphorylationEVPEANGSAGKRSKK
CCCCCCCCCCCHHHH		33.3925159151
247AcetylationEANGSAGKRSKKKKQ
CCCCCCCCHHHHHHH		53.8925953088
258PhosphorylationKKKQRKDSASEEEAH
HHHHHCCCCCHHHHH		36.4122817900
260PhosphorylationKQRKDSASEEEAHVG
HHHCCCCCHHHHHHC		49.8722817900
276PhosphorylationGKRKRRHSEVETDSK
CHHHHCCCCCCCCHH		41.3420164059
280PhosphorylationRRHSEVETDSKKKKM
HCCCCCCCCHHCCCC		51.2325850435
282PhosphorylationHSEVETDSKKKKMKL
CCCCCCCHHCCCCCC		54.5228176443
287SulfoxidationTDSKKKKMKLPEHPE
CCHHCCCCCCCCCCC		8.0721406390
288AcetylationDSKKKKMKLPEHPEG
CHHCCCCCCCCCCCC		70.5326051181
306AcetylationEDDEAPAKGKFNWKG
CCCCCCCCCCCCCHH		62.6725953088
312MalonylationAKGKFNWKGTIKAIL
CCCCCCCHHHHHHHH		47.4826320211
314PhosphorylationGKFNWKGTIKAILKQ
CCCCCHHHHHHHHHH		18.64-
320AcetylationGTIKAILKQAPDNEI
HHHHHHHHHCCCCCC		38.0025953088
320MalonylationGTIKAILKQAPDNEI
HHHHHHHHHCCCCCC		38.0032601280
340PhosphorylationRKKVLAQYYTVTDEH
HHHHHHHEEECCCCC		8.7628152594
341PhosphorylationKKVLAQYYTVTDEHH
HHHHHHEEECCCCCC		5.2228152594
342PhosphorylationKVLAQYYTVTDEHHR
HHHHHEEECCCCCCC		16.4028152594
344PhosphorylationLAQYYTVTDEHHRSE
HHHEEECCCCCCCCH		28.0628152594
3602-HydroxyisobutyrylationELLVIFNKKISKNPT
HEEEEECCCCCCCCC		40.51-
360AcetylationELLVIFNKKISKNPT
HEEEEECCCCCCCCC		40.5126051181
369AcetylationISKNPTFKLLKDKVK
CCCCCCHHHHHHHHH		56.2225953088
374UbiquitinationTFKLLKDKVKLVK--
CHHHHHHHHHCCC--		39.42-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LYAR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYAR_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LYAR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL23A_HUMANRPL23Aphysical
17353931
MBB1A_HUMANMYBBP1Aphysical
17353931
TWF2_HUMANTWF2physical
17353931
KRT85_HUMANKRT85physical
17353931
DHX57_HUMANDHX57physical
17353931
RL3_HUMANRPL3physical
17353931
TSR1_HUMANTSR1physical
17353931
BRX1_HUMANBRIX1physical
17353931
K1H1_HUMANKRT31physical
17353931
RS9_HUMANRPS9physical
17353931
NOG1_HUMANGTPBP4physical
17353931
RL18A_HUMANRPL18Aphysical
17353931
DHX9_HUMANDHX9physical
17353931
RS3A_HUMANRPS3Aphysical
17353931
RL21_HUMANRPL21physical
17353931
NAT10_HUMANNAT10physical
17353931
NPM_HUMANNPM1physical
17353931
NOG2_HUMANGNL2physical
17353931
DDX27_HUMANDDX27physical
17353931
EIF3I_HUMANEIF3Iphysical
17353931
KRT82_HUMANKRT82physical
17353931
EBP2_HUMANEBNA1BP2physical
17353931
RL31_HUMANRPL31physical
17353931
IMA5_HUMANKPNA1physical
17353931
SRP14_HUMANSRP14physical
17353931
DDX21_HUMANDDX21physical
17353931
ZHX1_HUMANZHX1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
P20L1_HUMANPHF20L1physical
21988832
BEND7_HUMANBEND7physical
25416956
XPF_HUMANERCC4physical
26344197
PRKRA_HUMANPRKRAphysical
21516116
NOG2_HUMANGNL2physical
26203195
RL23A_HUMANRPL23Aphysical
26203195
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYAR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY.

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